Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes
作者： Norma J. Greenfield , Regina Pietruszko
DOI: 10.1016/0005-2744(77)90005-5
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摘要: Abstract Human livre extracts show two major bands with aldehyde dehydrogenase (Aldehyde:NAD + oxidoreductase, EC 1.2.1.3) activity via starch gel electrophoresis at pH 7.0. Both have been purified to apparent homogeneity classical chromatography combined affinity on 5′-AMP-Sepharose 4B. The slower migratng band, enzyme 1, when assayed 9.5 has a low K m for NAD (8 μM) and high acetaldehyde (approx. 0.1 mM). It is very strongly inhibited by disulfiram 7.0 i of 0.2 μM. faster migrating 2, acetaldehyde, (2–3 μM 9.5), higher (70 not enzymes are similar the F1 F2 isozymes horse liver Eckfeldt et al. (Eckfeldt, J., Mope, L., Takio, K. Yonetani T. (1976) J. Biol. Chem. 251, 236–240) in molecular weight, subunit composition, amino acid composition extinction coefficient. Preliminary kinetic characterizations presented.
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